Global Subcellular Characterization of Protein Degradation Using Quantitative Proteomics*

التفاصيل البيبلوغرافية
العنوان: Global Subcellular Characterization of Protein Degradation Using Quantitative Proteomics*
المؤلفون: Kathryn J. Kirkwood, Angus I. Lamond, Tony Ly, Mark Larance, Yasmeen Ahmad
المصدر: Molecular & Cellular Proteomics : MCP
Larance, M, Ahmad, Y, Kirkwood, K J, Ly, T & Lamond, A I 2013, ' Global Subcellular Characterization of Protein Degradation Using Quantitative Proteomics ', Molecular and Cellular Proteomics, vol. 12, no. 3, pp. 638-650 . https://doi.org/10.1074/mcp.M112.024547
Molecular & Cellular Proteomics; Vol 12
Molecular & Cellular Proteomics
بيانات النشر: The American Society for Biochemistry and Molecular Biology, 2012.
سنة النشر: 2012
مصطلحات موضوعية: EXPRESSION, Proteomics, Proteasome Endopeptidase Complex, Proteome, Leupeptins, Quantitative proteomics, SPECTROMETRY-BASED PROTEOMICS, Immunoblotting, Intracellular Space, Protein degradation, Biology, Cysteine Proteinase Inhibitors, Biochemistry, UBIQUITIN, Mass Spectrometry, Analytical Chemistry, 03 medical and health sciences, 0302 clinical medicine, Cytosol, Cell Line, Tumor, Humans, AMINO-ACIDS, PHOSPHORYLATION, PROTEASOME, Molecular Biology, Cytoskeleton, 030304 developmental biology, Cell Nucleus, 0303 health sciences, STABILITY, Research, Membrane Proteins, LOCALIZATION, QUANTIFICATION, Protein subcellular localization prediction, Cell biology, Membrane protein, 030220 oncology & carcinogenesis, Proteolysis, Unfolded protein response, TURNOVER, Peptides
الوصف: Protein degradation provides an important regulatory mechanism used to control cell cycle progression and many other cellular pathways. To comprehensively analyze the spatial control of protein degradation in U2OS osteosarcoma cells, we have combined drug treatment and SILAC-based quantitative mass spectrometry with subcellular and protein fractionation. The resulting data set analyzed more than 74,000 peptides, corresponding to similar to 5000 proteins, from nuclear, cytosolic, membrane, and cytoskeletal compartments. These data identified rapidly degraded proteasome targets, such as PRR11 and high-lighted a feedback mechanism resulting in translation inhibition, induced by blocking the proteasome. We show this is mediated by activation of the unfolded protein response. We observed compartment-specific differences in protein degradation, including proteins that would not have been characterized as rapidly degraded through analysis of whole cell lysates. Bioinformatic analysis of the entire data set is presented in the Encyclopedia of Proteome Dynamics, a web-based resource, with proteins annotated for stability and subcellular distribution. Molecular & Cellular Proteomics 12: 10.1074/mcp.M112.024547, 638-650, 2013.
وصف الملف: application/pdf
اللغة: English
تدمد: 1535-9484
1535-9476
DOI: 10.1074/mcp.M112.024547
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b20b76ddcd358885541b7ef9e1ee7636
http://europepmc.org/articles/PMC3591657
Rights: OPEN
رقم الانضمام: edsair.doi.dedup.....b20b76ddcd358885541b7ef9e1ee7636
قاعدة البيانات: OpenAIRE
الوصف
تدمد:15359484
15359476
DOI:10.1074/mcp.M112.024547